scholarly journals Low molecular weight microtubule-associated proteins are light chains of microtubule-associated protein 1 (MAP 1).

1983 ◽  
Vol 80 (5) ◽  
pp. 1342-1346 ◽  
Author(s):  
R. B. Vallee ◽  
S. E. Davis
Keyword(s):  
Molecular Weight ◽  
Light Chains ◽  
Low Molecular Weight ◽  
Microtubule Associated Proteins ◽  
Associated Proteins

scholarly journals Two Related Subpellicular Cytoskeleton-associated Proteins inTrypanosoma brucei Stabilize Microtubules

2002 ◽  
Vol 13 (3) ◽  
pp. 1058-1070 ◽  
Author(s):  
Cécile Vedrenne ◽  
Christiane Giroud ◽  
Derrick R. Robinson ◽  
Sébastien Besteiro ◽  
Christophe Bosc ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Molecular Weight ◽  
Trypanosoma Brucei ◽  
Cold Resistance ◽  
Chinese Hamster ◽  
Low Molecular Weight ◽  
Microtubule Bundle ◽  
Microtubule Associated Proteins ◽  
Associated Proteins ◽  
Asymmetric Cytokinesis

The subpellicular microtubules of the trypanosome cytoskeleton are cross-linked to each other and the plasma membrane, creating a cage-like structure. We have isolated, from Trypanosoma brucei, two related low-molecular-weight cytoskeleton-associated proteins (15- and 17-kDa), called CAP15 and CAP17, which are differentially expressed during the life cycle. Immunolabeling shows a corset-like colocalization of both CAPs and tubulin. Western blot and electron microscope analyses show CAP15 and CAP17 labeling on detergent-extracted cytoskeletons. However, the localization of both proteins is restricted to the anterior, microtubule minus, and less dynamic half of the corset. CAP15 and CAP17 share properties of microtubule-associated proteins when expressed in heterologous cells (Chinese hamster ovary and HeLa), colocalization with their microtubules, induction of microtubule bundle formation, cold resistance, and insensitivity to nocodazole. When overexpressed inT. brucei, both CAP15 and CAP17 cover the whole subpellicular corset and induce morphological disorders, cell cycle-based abnormalities, and subsequent asymmetric cytokinesis.

Microtubule motors and other maps

1990 ◽  
Vol 48 (3) ◽  
pp. 1-1
Author(s):  
Richard B. Vallee
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cytoplasmic Dynein ◽  
Organelle Transport ◽  
Structural Components ◽  
Microtubule Associated Proteins ◽  
Microtubule Motors ◽  
Associated Proteins ◽  
The Subject ◽  
Intracellular Motility

Microtubules are involved in a number of forms of intracellular motility, including mitosis and bidirectional organelle transport. Purified microtubules from brain and other sources contain tubulin and a diversity of microtubule associated proteins (MAPs). Some of the high molecular weight MAPs - MAP 1A, 1B, 2A, and 2B - are long, fibrous molecules that serve as structural components of the cytamatrix. Three MAPs have recently been identified that show microtubule activated ATPase activity and produce force in association with microtubules. These proteins - kinesin, cytoplasmic dynein, and dynamin - are referred to as cytoplasmic motors. The latter two will be the subject of this talk.Cytoplasmic dynein was first identified as one of the high molecular weight brain MAPs, MAP 1C. It was determined to be structurally equivalent to ciliary and flagellar dynein, and to produce force toward the minus ends of microtubules, opposite to kinesin.

scholarly journals Identity and Origin of the ATPase activity associated with neuronal microtubules. I. The ATPase activity is associated with membrane vesicles.

1983 ◽  
Vol 96 (5) ◽  
pp. 1298-1305 ◽  
Author(s):  
D B Murphy ◽  
R R Hiebsch ◽  
K T Wallis
Keyword(s):  
Molecular Weight ◽  
Atpase Activity ◽  
High Molecular Weight ◽  
Brain Tissue ◽  
Membrane Vesicles ◽  
Microtubule Associated Proteins ◽  
In Vitro Assembly ◽  
Microtubule Protein ◽  
Associated Proteins

Microtubule protein purified from brain tissue by cycles of in vitro assembly-disassembly contains ATPase activity that has been postulated to be associated with microtubule-associated proteins (MAPs) and therefore significant for studies of microtubule-dependent motility. In this paper we demonstrate that greater than 90% of the ATPase activity is particulate in nature and may be derived from contaminating membrane vesicles. We also show that the MAPs (MAP-1, MAP-2, and tau factors) and other high molecular weight polypeptides do not contain significant amounts of ATPase activity. These findings do not support the concept of "brain dynein" or of MAPs with ATPase activity.

scholarly journals Association between endocrine pancreatic secretory granules and in-vitro-assembled microtubules is dependent upon microtubule-associated proteins.

1982 ◽  
Vol 93 (1) ◽  
pp. 164-174 ◽  
Author(s):  
K A Suprenant ◽  
W L Dentler
Keyword(s):  
Molecular Weight ◽  
Cyclic Amp ◽  
Light Microscopy ◽  
High Molecular Weight ◽  
Endocrine Pancreas ◽  
Secretory Granules ◽  
Dark Field ◽  
Microtubule Associated Proteins ◽  
Associated Proteins

By use of dark-field light microscopy, secretory granules isolated from the anglerfish endocrine pancreas were observed to attach to and release from microtubules assembled in vitro from brain homogenates. Secretory granules only bound to microtubules assembled in the presence of microtubule-associated proteins (MAPs) and not to microtubules assembled from purified tubulin. The addition of a MAP fraction to purified tubulin restored secretory granule binding. The secretory granules were released from MAP-containing microtubules by the addition of Mg-ATP but not by other nucleotides. The number of secretory granules bound to MAP-containing microtubules was increased in the presence of cyclic AMP. In addition to the associations of secretory granules with microtubules, MAP-containing microtubules also associated with each other. These laterally associated microtubules were dispersed by the addition of Mg-ATP. Electron micrographs confirmed that the associations between MAP-containing microtubules and secretory granules as well as the associations of microtubules with one another were mediated by the high molecular weight MAPs known to project from the surface of in-vitro-assembled microtubules.

scholarly journals Modulation of microtubule shape in vitro by high molecular weight microtubule associated proteins MAP1A, MAP1B, and MAP2

FEBS Letters ◽  
1996 ◽  
Vol 384 (2) ◽  
pp. 147-150 ◽  
Author(s):  
Barbara Pedrotti ◽  
Maura Francolini ◽  
Franco Cotelli ◽  
Khalid Islam
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Microtubule Associated Proteins ◽  
Associated Proteins

scholarly journals The Light Chains of Microtubule-Associated Proteins MAP1A and MAP1B Interact with α1-Syntrophin in the Central and Peripheral Nervous System

PLoS ONE ◽  
2012 ◽  
Vol 7 (11) ◽  
pp. e49722 ◽  
Author(s):  
Heike Fuhrmann-Stroissnigg ◽  
Rainer Noiges ◽  
Luise Descovich ◽  
Irmgard Fischer ◽  
Douglas E. Albrecht ◽  
...  
Keyword(s):  
Nervous System ◽  
Peripheral Nervous System ◽  
Light Chains ◽  
Microtubule Associated Proteins ◽  
Associated Proteins

High molecular weight microtubule-associated proteins: Purification by electro-elution and amino acid compositions

1986 ◽  
Vol 15 (4) ◽  
pp. 543-551 ◽  
Author(s):  
K. S. Kosik ◽  
S. F. Bakalis ◽  
D. J. Selkoe ◽  
M. W. Pierce ◽  
L. K. Duffy
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
High Molecular Weight ◽  
Amino Acid Compositions ◽  
Microtubule Associated Proteins ◽  
Associated Proteins

Cross-linking of microtubules by microtubule-associated proteins (MAPs) from the brine shrimp, Artemia

1989 ◽  
Vol 93 (1) ◽  
pp. 29-39
Author(s):  
E.J. Campbell ◽  
S.A. MacKinlay ◽  
T.H. MacRae
Keyword(s):  
Molecular Weight ◽  
Brine Shrimp ◽  
Cross Linking ◽  
Cross Link ◽  
Independent Manner ◽  
Western Blots ◽  
Microtubule Associated Proteins ◽  
Associated Proteins ◽  
Tubulin Protein

Microtubules induced with taxol to assemble in cell-free extracts of the brine shrimp, Artemia, are cross-linked by microtubule-associated proteins (MAPs). When the MAPs, extracted from taxol-stabilized microtubules with 1 M-NaCl are co-assembled with purified Artemia or mammalian neural tubulin, reconstitution of cross-linking between microtubules occurs. The most prominent non-tubulin protein associated with reconstituted cross-linked microtubules has a molecular weight of 49,000 but we cannot yet exclude the possibility that other proteins may be responsible for the cross-linking. Cross-linkers are separated by varying distances while cross-linked microtubules, prepared under different conditions, are 6.9-7.7 nm apart. Cross-linking of microtubules by MAPs occurs whether MAPs are added to assembling tubulin or to microtubules, and it is not disrupted by ATP. The MAPs are heat-sensitive and do not stabilize microtubules to cold. Immunological characterization of Artemia MAPs on Western blots indicates that Artemia lack MAP 1, MAP 2 and tau. Our results clearly demonstrate that Artemia contain novel MAPs with the ability to cross-link microtubules from phylogenetically disparate organisms in an ATP-independent manner.

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